MAP1B
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
PARK7
Gene Ontology Biological Process
- Ras protein signal transduction [TAS]
- activation of protein kinase B activity [IC]
- cellular response to glyoxal [IDA]
- cellular response to hydrogen peroxide [IDA]
- cellular response to oxidative stress [IDA, IMP]
- glycolate biosynthetic process [IDA]
- glyoxal catabolic process [IDA]
- hydrogen peroxide metabolic process [IDA]
- lactate biosynthetic process [IDA]
- methylglyoxal catabolic process to D-lactate [IDA]
- mitochondrion organization [ISS]
- negative regulation of TRAIL-activated apoptotic signaling pathway [IMP]
- negative regulation of apoptotic process [IDA]
- negative regulation of cell death [IDA]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [IMP]
- negative regulation of death-inducing signaling complex assembly [IC]
- negative regulation of extrinsic apoptotic signaling pathway [IMP]
- negative regulation of gene expression [IDA]
- negative regulation of hydrogen peroxide-induced cell death [IMP]
- negative regulation of hydrogen peroxide-induced neuron death [IDA]
- negative regulation of neuron apoptotic process [IDA]
- negative regulation of neuron death [IDA]
- negative regulation of oxidative stress-induced cell death [IDA]
- negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [IDA]
- negative regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- negative regulation of protein K48-linked deubiquitination [IDA]
- negative regulation of protein acetylation [IDA]
- negative regulation of protein binding [IDA, IGI, IMP]
- negative regulation of protein export from nucleus [IGI]
- negative regulation of protein kinase activity [IGI]
- negative regulation of protein phosphorylation [IGI]
- negative regulation of protein sumoylation [IDA]
- negative regulation of protein ubiquitination [IDA]
- negative regulation of ubiquitin-protein transferase activity [IDA]
- negative regulation of ubiquitin-specific protease activity [IDA]
- positive regulation of L-dopa biosynthetic process [IMP]
- positive regulation of L-dopa decarboxylase activity [IDA]
- positive regulation of androgen receptor activity [IMP]
- positive regulation of dopamine biosynthetic process [IC, IDA]
- positive regulation of gene expression [TAS]
- positive regulation of interleukin-8 production [IDA]
- positive regulation of mitochondrial electron transport, NADH to ubiquinone [IMP]
- positive regulation of peptidyl-serine phosphorylation [IMP]
- positive regulation of protein homodimerization activity [IDA]
- positive regulation of protein kinase B signaling [IC]
- positive regulation of protein localization to nucleus [IDA, IMP]
- positive regulation of pyrroline-5-carboxylate reductase activity [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IMP, TAS]
- positive regulation of superoxide dismutase activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IGI, IMP]
- positive regulation of transcription regulatory region DNA binding [IMP]
- positive regulation of tyrosine 3-monooxygenase activity [IDA]
- protein stabilization [IDA, IMP]
- regulation of TRAIL receptor biosynthetic process [IMP]
- regulation of androgen receptor signaling pathway [IDA]
- regulation of fibril organization [TAS]
- regulation of inflammatory response [ISS]
- regulation of mitochondrial membrane potential [IMP]
- regulation of neuron apoptotic process [IDA]
Gene Ontology Molecular Function- L-dopa decarboxylase activator activity [IDA]
- androgen receptor binding [IPI]
- core promoter binding [IC]
- cupric ion binding [IDA]
- cuprous ion binding [IDA]
- cytokine binding [IPI]
- double-stranded DNA binding [IDA]
- enzyme binding [IPI]
- glyoxalase (glycolic acid-forming) activity [IDA]
- glyoxalase III activity [IDA]
- identical protein binding [IPI]
- mRNA binding [IDA]
- oxidoreductase activity, acting on peroxide as acceptor [IDA]
- peptidase activity [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- receptor binding [IPI]
- repressing transcription factor binding [IPI]
- scaffold protein binding [IPI]
- single-stranded DNA binding [IDA]
- small protein activating enzyme binding [IPI]
- small protein conjugating enzyme binding [IPI]
- superoxide dismutase copper chaperone activity [IDA]
- transcription coactivator activity [IGI, TAS]
- transcription factor binding [IPI]
- tyrosine 3-monooxygenase activator activity [IDA]
- ubiquitin-specific protease binding [IPI]
- L-dopa decarboxylase activator activity [IDA]
- androgen receptor binding [IPI]
- core promoter binding [IC]
- cupric ion binding [IDA]
- cuprous ion binding [IDA]
- cytokine binding [IPI]
- double-stranded DNA binding [IDA]
- enzyme binding [IPI]
- glyoxalase (glycolic acid-forming) activity [IDA]
- glyoxalase III activity [IDA]
- identical protein binding [IPI]
- mRNA binding [IDA]
- oxidoreductase activity, acting on peroxide as acceptor [IDA]
- peptidase activity [IDA]
- protein binding [IPI]
- protein homodimerization activity [IDA]
- receptor binding [IPI]
- repressing transcription factor binding [IPI]
- scaffold protein binding [IPI]
- single-stranded DNA binding [IDA]
- small protein activating enzyme binding [IPI]
- small protein conjugating enzyme binding [IPI]
- superoxide dismutase copper chaperone activity [IDA]
- transcription coactivator activity [IGI, TAS]
- transcription factor binding [IPI]
- tyrosine 3-monooxygenase activator activity [IDA]
- ubiquitin-specific protease binding [IPI]
Co-localization
Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.
Publication
DJ-1 can inhibit microtubule associated protein 1 B formed aggregates.
Abnormal accumulation and aggregation of microtubule associated proteins (MAPs) plays an important role in the pathogenesis of neurodegenerative diseases. Loss-of-function mutation of DJ-1/Park7 can cause early onset of PD. DJ-1, a molecular chaperone, can inhibit α-synuclein aggregation. Currently, little is known whether or not loss of function of DJ-1 contributes to abnormal MAPs aggregation in neurodegenerative disorders such as PD.We ... [more]
Throughput
- Low Throughput
Additional Notes
- figure 1.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PARK7 MAP1B | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | 725354 | |
| MAP1B PARK7 | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | 725355 | |
| PARK7 MAP1B | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 725353 |
Curated By
- BioGRID